Protein phosphorylation in Streptomyces albus.
The phosphorylated proteins of Streptomyces albus, radioactively labeled with [32P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 protein species were found to be phosphorylated. With [32P]ATP as substrate cell free extracts phosphorylated endogenous proteins in vitro which were predominantly phosphorylated in vivo. From cell extract which exhibited active phosphorylated in vitro, a protein kinase has been partially purified. The kinase activity was identified in fractions corresponding to a 90 kDa protein.
Dobrová
Z
Z
Institute of Microbiology, Czechoslovak Academy of Sciences, Prague.
Jiresová
M
M
Petrík
T
T
Rysavý
P
P
Náprstek
J
J
Janecek
J
J
D001426:Bacterial Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology / Q000378:metabolism*
D001426:Bacterial Proteins; D011494:Protein Kinases